ID A0A6V8SIB4_9CLOT Unreviewed; 551 AA. AC A0A6V8SIB4; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 27-NOV-2024, entry version 14. DE RecName: Full=Hydroxylamine reductase {ECO:0000256|HAMAP-Rule:MF_00069}; DE EC=1.7.99.1 {ECO:0000256|HAMAP-Rule:MF_00069}; DE AltName: Full=Hybrid-cluster protein {ECO:0000256|HAMAP-Rule:MF_00069}; DE Short=HCP {ECO:0000256|HAMAP-Rule:MF_00069}; DE AltName: Full=Prismane protein {ECO:0000256|HAMAP-Rule:MF_00069}; GN Name=hcp {ECO:0000256|HAMAP-Rule:MF_00069}; GN ORFNames=bsdtw1_03081 {ECO:0000313|EMBL:GFP76969.1}; OS Clostridium fungisolvens. OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1604897 {ECO:0000313|EMBL:GFP76969.1, ECO:0000313|Proteomes:UP000580568}; RN [1] {ECO:0000313|EMBL:GFP76969.1, ECO:0000313|Proteomes:UP000580568} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TW1 {ECO:0000313|EMBL:GFP76969.1, RC ECO:0000313|Proteomes:UP000580568}; RA Ueki A., Tonouchi A.; RT "A new beta-1,3-glucan-decomposing anaerobic bacterium isolated from anoxic RT soil subjected to biological soil disinfestation."; RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reduction of hydroxylamine to form NH(3) and CC H(2)O. {ECO:0000256|HAMAP-Rule:MF_00069}. CC -!- CATALYTIC ACTIVITY: CC Reaction=A + NH4(+) + H2O = hydroxylamine + AH2 + H(+); CC Xref=Rhea:RHEA:22052, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15429, ChEBI:CHEBI:17499, CC ChEBI:CHEBI:28938; EC=1.7.99.1; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00069}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00069}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_00069}; CC -!- COFACTOR: CC Name=hybrid [4Fe-2O-2S] cluster; Xref=ChEBI:CHEBI:60519; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00069}; CC Note=Binds 1 hybrid [4Fe-2O-2S] cluster. {ECO:0000256|HAMAP- CC Rule:MF_00069}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00069}. CC -!- SIMILARITY: Belongs to the HCP family. {ECO:0000256|HAMAP- CC Rule:MF_00069}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:GFP76969.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BLZR01000001; GFP76969.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6V8SIB4; -. DR Proteomes; UP000580568; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0050418; F:hydroxylamine reductase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004601; F:peroxidase activity; IEA:TreeGrafter. DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:TreeGrafter. DR CDD; cd01914; HCP; 1. DR FunFam; 3.40.50.2030:FF:000001; Hydroxylamine reductase; 1. DR FunFam; 3.40.50.2030:FF:000002; Hydroxylamine reductase; 1. DR Gene3D; 1.20.1270.20; -; 2. DR Gene3D; 3.40.50.2030; -; 2. DR HAMAP; MF_00069; Hydroxylam_reduct; 1. DR InterPro; IPR004137; HCP/CODH. DR InterPro; IPR010048; Hydroxylam_reduct. DR InterPro; IPR016099; Prismane-like_a/b-sand. DR InterPro; IPR011254; Prismane-like_sf. DR InterPro; IPR016100; Prismane_a-bundle. DR NCBIfam; TIGR01703; hybrid_clust; 1. DR PANTHER; PTHR30109; HYDROXYLAMINE REDUCTASE; 1. DR PANTHER; PTHR30109:SF0; HYDROXYLAMINE REDUCTASE; 1. DR Pfam; PF03063; Prismane; 1. DR PIRSF; PIRSF000076; HCP; 1. DR SUPFAM; SSF56821; Prismane protein-like; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00069}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00069}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00069}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_00069}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00069}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00069}; Reference proteome {ECO:0000313|Proteomes:UP000580568}. FT BINDING 7 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 10 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 19 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 25 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 243 FT /ligand="hybrid [4Fe-2O-2S] cluster" FT /ligand_id="ChEBI:CHEBI:60519" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 267 FT /ligand="hybrid [4Fe-2O-2S] cluster" FT /ligand_id="ChEBI:CHEBI:60519" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 311 FT /ligand="hybrid [4Fe-2O-2S] cluster" FT /ligand_id="ChEBI:CHEBI:60519" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 403 FT /ligand="hybrid [4Fe-2O-2S] cluster" FT /ligand_id="ChEBI:CHEBI:60519" FT /note="via persulfide group" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 431 FT /ligand="hybrid [4Fe-2O-2S] cluster" FT /ligand_id="ChEBI:CHEBI:60519" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 456 FT /ligand="hybrid [4Fe-2O-2S] cluster" FT /ligand_id="ChEBI:CHEBI:60519" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 490 FT /ligand="hybrid [4Fe-2O-2S] cluster" FT /ligand_id="ChEBI:CHEBI:60519" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 492 FT /ligand="hybrid [4Fe-2O-2S] cluster" FT /ligand_id="ChEBI:CHEBI:60519" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT MOD_RES 403 FT /note="Cysteine persulfide" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" SQ SEQUENCE 551 AA; 61523 MW; 631EA7EB62A3EEC4 CRC64; MENSMFCYQC EQTFGGKGCT KSGVCGKTPE IANLQDLLIY QLKGISCYAK PLIEQGKIID KEIVKFVENG LFTTLTNVNF DAEVHVRLLK ESQKIKEALR DEAPEGKYPD QATYDLSDTK EEMLRDSVKA GIMYDEDLNE DVRSLRSTIL YGLKGVSAYG HQARFIGYNS QQVDNIYFLG LEATTNDDLT VEELIRMTMR VGDMSVEVMK TLDDANTTRY SNPSPHKVNV NIVKGPFIIV SGHDLRDLEM LLEQTEGKGI NIYTHGEMLP SHGYKELKKY KHLVGNYGSA WQNQQKEFDG IPGCILMTTN CLMRPRETYK DRIFSTSVVG WDGIKHIDMK EDGTKDFSEI INKALELGGF KESEEEKEIL VGFGHHATLS HAETIVNAVK EGKIRHFFLI GGCDGARPGR NYYTDFAKMV PEDCVILTLA CGKYRFNKLD FGTVAGLPRL LDVGQCNDAY SAVRIATALA DAFDTSVNAL PLTIVLSWYE QKAVADLLAL LSLGIKGMYL GPSLPAFISP NVLQYLVDTF NIKPISTPED DLRSSLKQAM C //